Surface topography of acetylcholinesterase in Langmuir and Langmuir-Blodgett films

Leila Dziri, Salah Boussaad, Shaopeng Wang, Roger M. Leblanc

Research output: Contribution to journalArticle

16 Citations (Scopus)

Abstract

The surface topography of the enzyme acetylcholinesterase was studied at the air/aqueous and the air/solid interfaces using the Brewster angle and the atomic force microscopies, respectively. Surface potentials of the enzyme monolayer have been measured in conjunction with the surface pressure. The surface potential and the surface dipole moment data show that the orientation of the molecular dipoles occurs before the orientation of the hydrophobic groups of the acetylcholinesterase monolayer. The variations of the surface potential observed at large molecular area suggest the presence of domains in the film. The Brewster angle images confirm the formation of domains at the air/aqueous interface. The size of these domains increases with decreasing the molecular area. Furthermore, the Brewster angle microscopy allowed us to detect a reversible formation of the domains upon the compression and the decompression of the monolayer. On the other hand, the atomic force microscope images of the Langmuir-Blodgett films show that the enzyme molecules are more close-packed at a surface pressure of 25 mN/m than at 20 mN/m. Size measurements of the enzyme particles indicate that acetylcholinesterase has an ellipsoidal shape and that the tetramer form of this enzyme is the most abundant.

Original languageEnglish (US)
Pages (from-to)6741-6748
Number of pages8
JournalJournal of Physical Chemistry B
Volume101
Issue number34
StatePublished - Aug 21 1997
Externally publishedYes

Fingerprint

Langmuir Blodgett films
Surface topography
Acetylcholinesterase
Langmuir-Blodgett films
enzymes
topography
Enzymes
Brewster angle
Surface potential
Monolayers
air
Air
pressure reduction
Dipole moment
Atomic force microscopy
Microscopic examination
dipole moments
Microscopes
microscopes
atomic force microscopy

ASJC Scopus subject areas

  • Physical and Theoretical Chemistry
  • Engineering(all)

Cite this

Surface topography of acetylcholinesterase in Langmuir and Langmuir-Blodgett films. / Dziri, Leila; Boussaad, Salah; Wang, Shaopeng; Leblanc, Roger M.

In: Journal of Physical Chemistry B, Vol. 101, No. 34, 21.08.1997, p. 6741-6748.

Research output: Contribution to journalArticle

Dziri, Leila ; Boussaad, Salah ; Wang, Shaopeng ; Leblanc, Roger M. / Surface topography of acetylcholinesterase in Langmuir and Langmuir-Blodgett films. In: Journal of Physical Chemistry B. 1997 ; Vol. 101, No. 34. pp. 6741-6748.
@article{04491ce79c04460e909cec5307f31deb,
title = "Surface topography of acetylcholinesterase in Langmuir and Langmuir-Blodgett films",
abstract = "The surface topography of the enzyme acetylcholinesterase was studied at the air/aqueous and the air/solid interfaces using the Brewster angle and the atomic force microscopies, respectively. Surface potentials of the enzyme monolayer have been measured in conjunction with the surface pressure. The surface potential and the surface dipole moment data show that the orientation of the molecular dipoles occurs before the orientation of the hydrophobic groups of the acetylcholinesterase monolayer. The variations of the surface potential observed at large molecular area suggest the presence of domains in the film. The Brewster angle images confirm the formation of domains at the air/aqueous interface. The size of these domains increases with decreasing the molecular area. Furthermore, the Brewster angle microscopy allowed us to detect a reversible formation of the domains upon the compression and the decompression of the monolayer. On the other hand, the atomic force microscope images of the Langmuir-Blodgett films show that the enzyme molecules are more close-packed at a surface pressure of 25 mN/m than at 20 mN/m. Size measurements of the enzyme particles indicate that acetylcholinesterase has an ellipsoidal shape and that the tetramer form of this enzyme is the most abundant.",
author = "Leila Dziri and Salah Boussaad and Shaopeng Wang and Leblanc, {Roger M.}",
year = "1997",
month = "8",
day = "21",
language = "English (US)",
volume = "101",
pages = "6741--6748",
journal = "Journal of Physical Chemistry B Materials",
issn = "1520-6106",
publisher = "American Chemical Society",
number = "34",

}

TY - JOUR

T1 - Surface topography of acetylcholinesterase in Langmuir and Langmuir-Blodgett films

AU - Dziri, Leila

AU - Boussaad, Salah

AU - Wang, Shaopeng

AU - Leblanc, Roger M.

PY - 1997/8/21

Y1 - 1997/8/21

N2 - The surface topography of the enzyme acetylcholinesterase was studied at the air/aqueous and the air/solid interfaces using the Brewster angle and the atomic force microscopies, respectively. Surface potentials of the enzyme monolayer have been measured in conjunction with the surface pressure. The surface potential and the surface dipole moment data show that the orientation of the molecular dipoles occurs before the orientation of the hydrophobic groups of the acetylcholinesterase monolayer. The variations of the surface potential observed at large molecular area suggest the presence of domains in the film. The Brewster angle images confirm the formation of domains at the air/aqueous interface. The size of these domains increases with decreasing the molecular area. Furthermore, the Brewster angle microscopy allowed us to detect a reversible formation of the domains upon the compression and the decompression of the monolayer. On the other hand, the atomic force microscope images of the Langmuir-Blodgett films show that the enzyme molecules are more close-packed at a surface pressure of 25 mN/m than at 20 mN/m. Size measurements of the enzyme particles indicate that acetylcholinesterase has an ellipsoidal shape and that the tetramer form of this enzyme is the most abundant.

AB - The surface topography of the enzyme acetylcholinesterase was studied at the air/aqueous and the air/solid interfaces using the Brewster angle and the atomic force microscopies, respectively. Surface potentials of the enzyme monolayer have been measured in conjunction with the surface pressure. The surface potential and the surface dipole moment data show that the orientation of the molecular dipoles occurs before the orientation of the hydrophobic groups of the acetylcholinesterase monolayer. The variations of the surface potential observed at large molecular area suggest the presence of domains in the film. The Brewster angle images confirm the formation of domains at the air/aqueous interface. The size of these domains increases with decreasing the molecular area. Furthermore, the Brewster angle microscopy allowed us to detect a reversible formation of the domains upon the compression and the decompression of the monolayer. On the other hand, the atomic force microscope images of the Langmuir-Blodgett films show that the enzyme molecules are more close-packed at a surface pressure of 25 mN/m than at 20 mN/m. Size measurements of the enzyme particles indicate that acetylcholinesterase has an ellipsoidal shape and that the tetramer form of this enzyme is the most abundant.

UR - http://www.scopus.com/inward/record.url?scp=0031213043&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0031213043&partnerID=8YFLogxK

M3 - Article

VL - 101

SP - 6741

EP - 6748

JO - Journal of Physical Chemistry B Materials

JF - Journal of Physical Chemistry B Materials

SN - 1520-6106

IS - 34

ER -